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    Triad3A Regulates Synaptic Strength by Ubiquitination of Arc

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    Publication date
    2014-06-18
    Author
    Mabb, A.M.
    Je, H.S.
    Wall, M.J.
    Robinson, C.G.
    Larsen, R.S.
    Qiang, Y.
    Corrêa, Sonia A.L.
    Ehlers, M.D.
    Keyword
    Triad3A; Regulation; Synaptic strength; Arc induction; Ubiquitination; Glutamatergic synapses; Synaptic plasticity
    Peer-Reviewed
    yes
    
    Metadata
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    Abstract
    Activity-dependent gene transcription and protein synthesis underlie many forms of learning-related synaptic plasticity. At excitatory glutamatergic synapses, the immediate early gene product Arc/ Arg3.1 couples synaptic activity to postsynaptic endocytosis of AMPA-type glutamate receptors. Although the mechanisms for Arc induction have been described, little is known regarding the molecular machinery that terminates Arc function. Here, we demonstrate that the RING domain ubiquitin ligase Triad3A/RNF216 ubiquitinates Arc, resulting in its rapid proteasomal degradation. Triad3A associates with Arc, localizes to clathrin-coated pits, and is associated with endocytic sites in dendrites and spines. In the absence of Triad3A, Arc accumulates, leading to the loss of surface AMPA receptors. Furthermore, loss of Triad3A mimics and occludes Arc-dependent forms of synaptic plasticity. Thus, degradation of Arc by clathrin-localized Triad3A regulates the availability of synaptic AMPA receptors and temporally tunes Arc-mediated plasticity at glutamatergic synapses.
    URI
    http://hdl.handle.net/10454/8080
    Version
    Accepted Manuscript
    Citation
    Mabb AM, Je HS, Wall MJ et al. (2014) Triad3A Regulates Synaptic Strength by Ubiquitination of Arc. Neuron, 82 (6): 1299–1316
    Link to publisher’s version
    http://dx.doi.org/10.1016/j.neuron.2014.05.016
    Type
    Article
    Notes
    A final draft copy of this article is not yet available.
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    Life Sciences Publications

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